Type II thioesterase restores activity of a NRPS module stalled with an aminoacyl-S-enzyme that cannot be elongated

Chembiochem. 2004 Sep 6;5(9):1290-3. doi: 10.1002/cbic.200400077.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids / chemistry
  • Aminohydrolases / metabolism*
  • Cysteamine / chemistry
  • Cysteamine / metabolism
  • Fatty Acid Synthases / metabolism*
  • Hydrolysis
  • Peptide Synthases / metabolism*
  • Thiolester Hydrolases / metabolism*

Substances

  • Amino Acids
  • Cysteamine
  • Fatty Acid Synthases
  • Thiolester Hydrolases
  • thioesterase II
  • Aminohydrolases
  • Peptide Synthases
  • non-ribosomal peptide synthase